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Related Concept Videos

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Laminins are the Adhesive Proteins of Basal Lamina00:55

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
Anchoring Junctions01:03

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...

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Related Experiment Video

Updated: Jul 8, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Lsc activity is controlled by oligomerization and regulates integrin adhesion.

Jiancheng Hu1, Pamela Strauch, Anatoly Rubtsov

  • 1Integrated Department of Immunology, University of Colorado Health Sciences Center and National Jewish Medical and Research Center, Denver, CO 80206, USA.

Molecular Immunology
|December 26, 2007
PubMed
Summary

Leukocyte signaling complex (Lsc) forms a large oligomer in B lymphocytes, regulating cell adhesion and migration. Disrupting this complex activates Lsc, impairing cell adhesion and causing cell rounding.

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Last Updated: Jul 8, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
10:34

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Published on: April 23, 2017

Assay of Adhesion Under Shear Stress for the Study of T Lymphocyte-Adhesion Molecule Interactions
07:40

Assay of Adhesion Under Shear Stress for the Study of T Lymphocyte-Adhesion Molecule Interactions

Published on: June 29, 2016

Area of Science:

  • Cell Biology
  • Immunology
  • Molecular Biology

Background:

  • Leukocyte signaling complex (Lsc) is crucial for leukocyte migration and B lymphocyte adhesion.
  • Lsc acts as an effector for G protein-coupled receptors, activating RhoA.
  • Defects in Lsc lead to impaired leukocyte migration and inefficient adhesion resolution in B cells.

Purpose of the Study:

  • To investigate the physiological state and function of Lsc in primary B lymphocytes.
  • To determine the role of Lsc oligomerization in its functional activities.
  • To elucidate the localization and mechanism of Lsc during cell migration.

Main Methods:

  • Analysis of Lsc molecular weight and oligomeric state in primary B lymphocytes.
  • Experimental manipulation of Lsc oligomer assembly.
  • Observation of Lsc localization during cell migration on integrin ligands.
  • Assessment of cell morphology and integrin-mediated adhesion.

Main Results:

  • Lsc physiologically exists as a large molecular weight complex, likely a homo-tetramer, in primary B lymphocytes.
  • Interference with Lsc oligomer assembly activates Lsc's RhoA-activating function.
  • Disruption of Lsc oligomerization leads to cell rounding and inhibited integrin-mediated adhesion.
  • During migration, Lsc accumulates at the rear of cells, suggesting a role in adhesion resolution.

Conclusions:

  • Lsc functions as a homo-tetrameric complex in B lymphocytes.
  • Lsc oligomerization is critical for regulating its functional activities, including RhoA activation.
  • Lsc plays a key role at the trailing edge of migrating cells, resolving integrin-mediated adhesion.